CN106632599A - Anti-tumor enzyme hydrolyzed cyclina sinensis oligopeptide - Google Patents
Anti-tumor enzyme hydrolyzed cyclina sinensis oligopeptide Download PDFInfo
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- CN106632599A CN106632599A CN201610326513.0A CN201610326513A CN106632599A CN 106632599 A CN106632599 A CN 106632599A CN 201610326513 A CN201610326513 A CN 201610326513A CN 106632599 A CN106632599 A CN 106632599A
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- 108010038807 Oligopeptides Proteins 0.000 title claims abstract description 30
- 102000015636 Oligopeptides Human genes 0.000 title claims abstract description 30
- 230000000259 anti-tumor effect Effects 0.000 title claims abstract description 20
- 102000004190 Enzymes Human genes 0.000 title abstract description 10
- 108090000790 Enzymes Proteins 0.000 title abstract description 10
- 241000514743 Cyclina sinensis Species 0.000 title abstract description 5
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 4
- 238000004128 high performance liquid chromatography Methods 0.000 abstract description 3
- 235000013305 food Nutrition 0.000 abstract description 2
- 238000000108 ultra-filtration Methods 0.000 abstract description 2
- 230000002929 anti-fatigue Effects 0.000 abstract 1
- 235000013376 functional food Nutrition 0.000 abstract 1
- 238000000746 purification Methods 0.000 abstract 1
- 239000002994 raw material Substances 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 20
- 239000004365 Protease Substances 0.000 description 10
- 230000000694 effects Effects 0.000 description 9
- 108091005804 Peptidases Proteins 0.000 description 7
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 235000019419 proteases Nutrition 0.000 description 7
- 206010060862 Prostate cancer Diseases 0.000 description 5
- 208000000236 Prostatic Neoplasms Diseases 0.000 description 5
- 230000006907 apoptotic process Effects 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- 239000003814 drug Substances 0.000 description 4
- 108090000526 Papain Proteins 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 239000011543 agarose gel Substances 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 238000004108 freeze drying Methods 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 235000019834 papain Nutrition 0.000 description 3
- 229940055729 papain Drugs 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 230000035755 proliferation Effects 0.000 description 3
- 229920002683 Glycosaminoglycan Polymers 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 102000057297 Pepsin A Human genes 0.000 description 2
- 108090000284 Pepsin A Proteins 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 238000005227 gel permeation chromatography Methods 0.000 description 2
- 230000014509 gene expression Effects 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 229940111202 pepsin Drugs 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 210000001835 viscera Anatomy 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 208000032791 BCR-ABL1 positive chronic myelogenous leukemia Diseases 0.000 description 1
- 208000010833 Chronic myeloid leukaemia Diseases 0.000 description 1
- 241001522252 Crassostrea rivularis Species 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- PWUMCBLVWPCKNO-MGHWNKPDSA-N Ile-Leu-Tyr Chemical compound CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 PWUMCBLVWPCKNO-MGHWNKPDSA-N 0.000 description 1
- 241000446313 Lamella Species 0.000 description 1
- 241000237852 Mollusca Species 0.000 description 1
- 208000033761 Myelogenous Chronic BCR-ABL Positive Leukemia Diseases 0.000 description 1
- 241000620877 Ruditapes philippinarum Species 0.000 description 1
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 1
- 101000693530 Staphylococcus aureus Staphylokinase Proteins 0.000 description 1
- 208000005718 Stomach Neoplasms Diseases 0.000 description 1
- 241000237551 Veneridae Species 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 208000009956 adenocarcinoma Diseases 0.000 description 1
- 239000003098 androgen Substances 0.000 description 1
- 230000000954 anitussive effect Effects 0.000 description 1
- 230000001857 anti-mycotic effect Effects 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 239000002543 antimycotic Substances 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 229940041181 antineoplastic drug Drugs 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 235000006708 antioxidants Nutrition 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 238000005202 decontamination Methods 0.000 description 1
- 230000003588 decontaminative effect Effects 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000005238 degreasing Methods 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 230000000857 drug effect Effects 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000004043 dyeing Methods 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 235000019634 flavors Nutrition 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 206010017758 gastric cancer Diseases 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000009413 insulation Methods 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 235000004213 low-fat Nutrition 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 210000001501 megacaryocyte Anatomy 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000002438 mitochondrial effect Effects 0.000 description 1
- 210000001700 mitochondrial membrane Anatomy 0.000 description 1
- 230000004660 morphological change Effects 0.000 description 1
- 239000005445 natural material Substances 0.000 description 1
- 230000001151 other effect Effects 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- INAAIJLSXJJHOZ-UHFFFAOYSA-N pibenzimol Chemical compound C1CN(C)CCN1C1=CC=C(N=C(N2)C=3C=C4NC(=NC4=CC=3)C=3C=CC(O)=CC=3)C2=C1 INAAIJLSXJJHOZ-UHFFFAOYSA-N 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 201000007094 prostatitis Diseases 0.000 description 1
- 238000001959 radiotherapy Methods 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 235000015170 shellfish Nutrition 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 201000011549 stomach cancer Diseases 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 238000004627 transmission electron microscopy Methods 0.000 description 1
- -1 trypsase Proteins 0.000 description 1
- 208000029584 urinary system neoplasm Diseases 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
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- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention discloses an anti-tumor enzyme hydrolyzed cyclina sinensis oligopeptide. The anti-tumor enzyme hydrolyzed cyclina sinensis oligopeptide is prepared from a raw material cyclina sinensis by ultrafiltration and HPLC (high performance liquid chromatography) purification, the amino acid sequence of the oligopeptide is Ile-Leu-Tyr-Met-Pro, and the molecular weight is 635.82Da. The oligopeptide has anti-tumor activity, and can be developed as anti-fatigue functional food or healthcare food.
Description
Technical field
The present invention relates to a kind of marine bioactivity oligopeptides, and in particular to a kind of antitumor enzymolysis oligopeptide of clam.
Background technology
The incidence of disease of prostate cancer ranks first in male malignancy middle position, is apt to occur in elderly men.In China, prostate
Cancer morbidity occupies the first place of Patients with Urinary System Tumors in ascendant trend year by year, the health of serious threat elderly men.Traditional treatment side
Method is as unsatisfactory such as operation, radiotherapy and cold therapy and other effects, and recurrence rate is higher, and when the prostate cancer conversion of recurrence
For non-androgen-dependent when, treatment will be more difficult；And chemotherapeutics is produced after drug resistance, curative effect is worse and toxic and side effect is bright
It is aobvious.Therefore, finding antiprostate cancer becomes the focus that scholars study.Ocean is one of discovery new anticancer drug rich
Rich resource treasure-house, various ocean oligopeptides, glycosaminoglycan etc. all have the physiologically active such as antitumor, antiviral, antimycotic.From double
Clam oligopeptides Mere15, the Ruditapes philippinarum oligopeptides extracted in shell shellfish is to people's chronic myelogenous leukemia K562 cells, prostatitis
Adenocarcinoma cell has inhibited proliferation, and causes Concentration dependent cell apoptosis；From the glycosaminoglycan tool that Crassostrea rivularis is extracted
There is inside and outside antitumor activity, the growth of K562, CNE-2Z, Hela cell not only can be suppressed, also mouse is damaged to CTX and exempted from
Epidemic disease function has certain repair.Clam（Cyclina sinensis）Belong to Mollusca, gill lamella guiding principle, different tooth subclass,
Curtain clam mesh, Veneridae, the unrighted acid containing high protein, low fat and high-load, delicious flavour, with good nutriture value
Value.Clam it is among the people be used as medicine have a long history, be a kind of important marine drug, with softening and resolving hard mass, heat-clearing and damp-drying drug and
Antitussive effect.The polysaccharide that Changxing J etc. are extracted from clam has anti-oxidant and liver-protecting activity, to human gastric cancer BGC-
The growth of 823 cells has strong inhibitory action.However, current report simultaneously with regard to the extraction of clam oligopeptides and the research of activity
Seldom, this experiment adopts protease hydrolyzed clam internal organ, Jing orthogonal experiments to obtain optimum enzymolysis condition, separated purifying, screening
Go out active oligopeptide, study the activity of its external anti-human prostate cancer DU-145 cell, to for the preparation of clam active oligopeptide and
Antitumaous effect research provides experimental basis.
The content of the invention
The technical problem to be solved is to provide a kind of antitumor enzymolysis oligopeptide of clam with antitumor efficacy.
The present invention is for the solution technical scheme taken of above-mentioned technical problem：The amino acid sequence of the oligopeptides is Ile-
Leu-Tyr-Met-Pro（ILYMP）, molecular weight is 635.82Da.
The peptide is prepared in the following way：
1）Clam homogenate is taken, with organized enzyme at peak enzymolysis-ability temperature and pH value condition, plus the U/g of protease 200 ~ 12000, guarantor
4 ~ 10 h of temperature are digested；Then inactivate afterwards, be centrifuged under conditions of 0 ~ 4 oC, 12000 r/min, take supernatant；
2）The supernatant digested under optimal enzyme and optimum enzymatic hydrolysis condition is taken, is surpassed with the milipore filter that molecular cut off is 3 ku
Filter；
3）Taking ultrafiltration component carries out agarose gel chromatography separation, concentration：0.01 ~ 0.5g/mL, takes supernatant and crosses 0.22 after centrifugation
M filter membranes, are eluted；Collect eluted product, freeze-drying；
4）Take component and cross the HPLC further antitumor enzymolysis oligopeptides of isolated clam.
Compared with prior art, a kind of advantage of the antitumor enzymolysis oligopeptide of clam that the present invention is provided is：Work of the present invention
Skill is scientific and reasonable, simple to operate, with the antitumor enzymolysis oligopeptide of clam（CSOP）The increase of concentration, the prolongation of action time, DU-
The proliferation inhibition rate of 145 cells substantially rises；Observation, AO/EB fluorescent stainings, the fluorescence of Hoechst 33258 under inverted microscope
Dyeing and transmission electron microscopy experiment show that the morphological change of apoptosis occurs in cell；Flow cytometry results show, cell morning
Phase apoptosis rate and mitochondrial membrane potential decline shared percentage and increase, and as CSOP concentration increases, early apoptosis rate increase compared with
For obvious, its film potential declines more notable, i.e. indication mitochondrial apoptosis signal path withers in the DU-145 cells that CSOP is induced
Play an important role during dying.Meanwhile, the antitumor enzymolysis oligopeptide of clam prepared by the present invention is natural material Jing enzymolysis systems
, safe and free of toxic and side effects, significantly, the antitumor enzymolysis oligopeptide of clam can be used as anti-prostate cancer medicine, work(for antitumor activity
Energy food is developed.
Description of the drawings
Fig. 1 sheets are inventive embodiments schematic arrangement；
Fig. 2 sheets are inventive embodiments agarose Gel column eluting peak schematic diagram；
Fig. 3 sheets are inventive embodiments oligopeptides component high-efficient liquid phase chromatogram at 280nm；
Fig. 4 sheets are inhibited proliferation comparison diagram of the inventive embodiments oligopeptides to DU-145 cells；
Fig. 5 is expression schematic diagram of the embodiment of the present invention to DU-145 cell nm23H1 albumen.
Specific embodiment
The present invention is described in further detail with reference to embodiments.
Embodiment：
A kind of antitumor enzymolysis oligopeptide preparation technology flow process of clam is as follows：
1）The preparation of sample
Clam cleaned, is shelled, taking internal organ, and degreasing is soaked with the NaoH solution of 0.1 mol/L, being gently mixed in distilled water
Decontamination, it is standby after the pure water homogenate of the volume that doubles.
2）The enzymolysis of clam：Take 10.0 g homogenised samples respectively, with alkali protease, trypsase, papain, in
Property protease and pepsin this 5 kinds of enzymes be for examination enzyme, at respective peak enzymolysis-ability temperature and pH value condition（It is shown in Table 1）, plus
Protease 1200-1800 U/g, insulation 1-6 h are digested.Inactivate 15 min after end, 4 oC, 12000 r/min centrifugation 10
Min, takes supernatant.
The peak enzymolysis-ability temperature and pH of the different protease of table 1
| Enzyme | Hydrolysis temperature（℃） | Enzymolysis pH |
| Alkali protease | 45.0 | 10.0 |
| Trypsase | 37.0 | 8.0 |
| Papain | 60.0 | 6.0 |
| Neutral proteinase | 45.0 | 7.0 |
| Pepsin | 37.0 | 2.0 |
Preferably, optimum enzyme is papain.Solid-liquid ratio is 1:4, pH value is 7.0, enzyme concentration be 1500 U/g, temperature
For 45.0 DEG C, enzymolysis time is 4 h.
3）Clam antitumor enzymolysis oligopeptide is isolated and purified：The above-mentioned ku molecule section enzymolysis liquids of supernatant ＜ 3 will be chosen to be carried out
Lower step purifying.Detailed process is：
Taking the lyophilized sample of the ku molecules sections of ＜ 3 carries out agarose gel chromatography, occurs three peaks, i.e. peak 1, the and of peak 2 at 280 nm
Peak 3, is shown in Fig. 2, collects each peak component, freeze-drying.Mtt assay shows that peak 1 and peak 3 are preferable to the inhibitory activity of DU-145 cells.
Collect the freeze-drying of peak 1.Peak 1 is clam enzymolysis oligopeptide, and the retention time at the peak is about 12 min, peak area 16.32, peak height
The sequencing of 1999.79, Jing N-terminals show that the amino acid sequence of the peptide is：Ile-Leu-Tyr-Met-Pro, molecular weight 635.82Da.
MTT results after CSOP effect DU-145 cells are shown in Fig. 4.Clam enzymolysis oligopeptide（That is CSOP）The increase of concentration, work
With the prolongation of time, increment inhibiting rate IR substantially rises.When CSOP concentration is 2 mg/mL, action time is 24 h, and IR is 9.89
±0.49 %；And working as concentration for 15 mg/mL, the h of action time 72, IR reach 84.17 ± 4.21 %, IC50For 5.36 ± 0.27
Mg/mL, with statistical significance compared with control group（P＜ 0.05）.
Nm23H1 protein positive expressions are brown structure occur in cytoplasm.The normal DU-145 cells B 2mg/mL of A
CSOP group DU-145 cells, C 8mg/mL CSOP group DU-145 cells, D 12mg/mL CSOP group DU-145 cells.Control group
It is in light brown in most cells endochylema, respective cells present negative（See A）.And with the increase of CSOP activities, the visual field
Under cell quantity significantly reduce, intracytoplasmic positive site color is gradually deepened, and occurs in that megacaryocyte, part nucleus
In pyknosis state.
Finally, in addition it is also necessary to it is noted that listed above is only a specific embodiment of the invention.Obviously, the present invention
Above example is not limited to, there can also be many deformations.One of ordinary skill in the art can be straight from present disclosure
The all deformations derived or associate are connect, protection scope of the present invention is considered as.
SEQUENCE LISTING
<110>Oceanography Institute Of Zhejiang
<120>A kind of antitumor enzymolysis oligopeptide of clam
<130> zjou-yzs-01
<160> 1
<170> PatentIn version 3.5
<210> 1
<211> 5
<212> PRT
<213>It is artificial synthesized
<400> 1
Ile Leu Tyr Met Pro
1 5
Claims (1)
1. the antitumor enzymolysis oligopeptide of a kind of clam, it is characterised in that：The amino acid sequence of the oligopeptides is Ile-Leu-Tyr-Met-
Pro, molecular weight is 635.82Da.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201610326513.0A CN106632599B (en) | 2016-05-17 | 2016-05-17 | clam antineoplastic enzymolysis oligopeptides |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201610326513.0A CN106632599B (en) | 2016-05-17 | 2016-05-17 | clam antineoplastic enzymolysis oligopeptides |
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| Publication Number | Publication Date |
|---|---|
| CN106632599A true CN106632599A (en) | 2017-05-10 |
| CN106632599B CN106632599B (en) | 2020-01-31 |
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|---|---|---|---|
| CN201610326513.0A Active CN106632599B (en) | 2016-05-17 | 2016-05-17 | clam antineoplastic enzymolysis oligopeptides |
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| Country | Link |
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Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104212861A (en) * | 2013-05-29 | 2014-12-17 | 浙江海洋学院 | Preparation method of ruditapes philippinarum oligopeptide and application in resisting prostate cancer |
-
2016
- 2016-05-17 CN CN201610326513.0A patent/CN106632599B/en active Active
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104212861A (en) * | 2013-05-29 | 2014-12-17 | 浙江海洋学院 | Preparation method of ruditapes philippinarum oligopeptide and application in resisting prostate cancer |
Non-Patent Citations (1)
| Title |
|---|
| 闫海强: "抗肿瘤活性青蛤多肽的提取工艺研究", 《安徽农业科学》 * |
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